Abstract
Drugs inhibiting Aldose Reductase (AR) may have a profound therapeutic impact for patients suffering for diabetes Mellitus. However, a prerequisite for such a long term treatment is the absence of side effects. For the drug design, the knowledge of the structure of AR will be a most useful contribution and will answer a number of puzzling facts such as the surprisingly large number of aldehydes which are substrates for AR. In this account, we present preliminary results of a structural study of pig lens Aldose Reductase.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Fenn, J.B., Mann, M., Meng, CK., Wong, S.F., and Whitehouse,C.M., Electrospray Ionization for Mass Spectrometry of Large Biomolecules, Science, 246: 64, (1989).
Gilbert, L.M., and Gilbert, G.A., Sedimentation Velocity Measurement of Protein Association, Meth. Enzymol.,27: 273, (1973) .
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1990 Plenum Press, New York
About this chapter
Cite this chapter
Rondeau, JM. et al. (1990). Structural Studies of Pig Lens Aldose Reductase: Reversible Dimerization of the Enzyme. In: Weiner, H., Wermuth, B., Crabb, D.W. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 3. Advances in Experimental Medicine and Biology, vol 284. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5901-2_14
Download citation
DOI: https://doi.org/10.1007/978-1-4684-5901-2_14
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4684-5903-6
Online ISBN: 978-1-4684-5901-2
eBook Packages: Springer Book Archive